The DOI matches its Crossref record; 80 of the 80 references it cites were found in a registry or an index.
ERM proteins: From cellular architecture to cell signaling
Abstract
ERM (ezrin/radixin/moesin) proteins, concentrated in actin rich cell‐surface structures, cross‐link actin filaments with the plasma membrane. They are involved in the formation of microvilli, cell‐cell adhesion, maintenance of cell shape, cell motility and membrane trafficking. Recent analyses reveal that they are not only involved in cytoskeleton organization but also in signaling pathway. They play an important role in the activation of members of the Rho family by recruiting their regulators. The functions of ERM proteins are regulated by their conformational charges: the intramolecular interaction between the N‐ and C‐terminal domains of ERM proteins charges masks several binding sites, leading to a dormant protein. Different activation signals regulate ERM proteins functions by modulating these intramolecular interactions. The involvement of ERM proteins in many signaling pathways has led to study their role during development of different species.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Rouleau, G. A., Merel, P., Lutchman, M., Sanson, M., Zucman, J., Marineau, C., Hoang-Xuan, K., Demczuk, S., Desmaze, C., Plougastel, B., et al. (1993) · Nature · doi:10.1038/363515a0 · Cited by 1,420
Trofatter, J. (1993) · Cell · doi:10.1016/0092-8674(93)90406-g · Cited by 1,403
Matsui, T., Maeda, M., Doi, Y., Yonemura, S., Amano, M., Kaibuchi, K., Tsukita, S., & Tsukita, S. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.3.647 · Cited by 864
Tsukita, S., Oishi, K., Sato, N., Sagara, J., Kawai, A., & Tsukita, S. (1994) · The Journal of cell biology · doi:10.1083/jcb.126.2.391 · Cited by 779
A kinase-regulated PDZ-domain interaction controls endocytic sorting of the β2-adrenergic receptor
Cao, T. T., Deacon, H. W., Reczek, D., Bretscher, A., & von Zastrow, M. (1999) · Nature · doi:10.1038/45816 · Cited by 673
Epidermal growth factor induces rapid tyrosine phosphorylation of proteins in A431 human tumor cells
Hunter, T., & Cooper, J. A. (1981) · Cell · doi:10.1016/0092-8674(81)90100-8 · Cited by 650
Yonemura, S., Hirao, M., Doi, Y., Takahashi, N., Kondo, T., Tsukita, S., & Tsukita, S. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.4.885 · Cited by 613
Pearson, M. A., Reczek, D., Bretscher, A., & Karplus, P. A. (2000) · Cell · doi:10.1016/s0092-8674(00)80836-3 · Cited by 604
Hirao, M., Sato, N., Kondo, T., Yonemura, S., Monden, M., Sasaki, T., Takai, Y., Tsukita, S., & Tsukita, S. (1996) · The Journal of cell biology · doi:10.1083/jcb.135.1.37 · Cited by 593
Reczek, D., Berryman, M., & Bretscher, A. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.1.169 · Cited by 578
Cited by
Yu, Y., Khan, J., Khanna, C., Helman, L., Meltzer, P. S., & Merlino, G. (2004) · Nature Medicine · doi:10.1038/nm966 · Cited by 525
Shi-Wen, X., Chen, Y., Denton, C. P., Eastwood, M., Renzoni, E. A., Bou-Gharios, G., Pearson, J. D., Dashwood, M., du Bois, R. M., Black, C. M., et al. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-12-0902 · Cited by 356
Small molecule inhibitors of ezrin inhibit the invasive phenotype of osteosarcoma cells
Bulut, G., Hong, S.-H., Chen, K., Beauchamp, E. M., Rahim, S., Kosturko, G. W., Glasgow, E., Dakshanamurthy, S., Lee, H.-S., Daar, I., et al. (2012) · Oncogene · doi:10.1038/onc.2011.245 · Cited by 179
Yang, H.-S., & Hinds, P. W. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00135-7 · Cited by 75
TRPC-mediated actin-myosin contraction is critical for BBB disruption following hypoxic stress
Hicks, K., O'Neil, R. G., Dubinsky, W. S., & Brown, R. C. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00458.2009 · Cited by 70
Metadata
- Authors
- Louvet‐Vallée, S.
- Venue
- Biology of the Cell
- Publisher
- Wiley
- Published
- 2000-08
- Volume
- 92
- Issue
- 5
- Pages
- 305-316
- ISSN
- 0248-4900 (ISSN-L)
- 1768-322X
- OpenAlex
- W2036631473
- Cited by
- 318
- References
- 80
- FWCI
- 3.60
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: ERM proteins: From cellular architecture to cell signaling. https://app.cochat.ai/papers/10.1016/s0248-4900(00)01078-9
- The paper
- Louvet‐Vallée, S. (2000). ERM proteins: From cellular architecture to cell signaling. Biology of the Cell. https://doi.org/10.1016/s0248-4900(00)01078-9
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.